ID PURA2_HUMAN Reviewed; 456 AA. AC P30520; B1AQM5; Q96EG7; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 3. DT 27-MAR-2024, entry version 218. DE RecName: Full=Adenylosuccinate synthetase isozyme 2 {ECO:0000255|HAMAP-Rule:MF_03127}; DE Short=AMPSase 2 {ECO:0000255|HAMAP-Rule:MF_03127}; DE Short=AdSS 2 {ECO:0000255|HAMAP-Rule:MF_03127}; DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03127}; DE AltName: Full=Adenylosuccinate synthetase, acidic isozyme {ECO:0000255|HAMAP-Rule:MF_03127}; DE AltName: Full=Adenylosuccinate synthetase, liver isozyme {ECO:0000255|HAMAP-Rule:MF_03127}; DE Short=L-type adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03127}; DE AltName: Full=IMP--aspartate ligase 2 {ECO:0000255|HAMAP-Rule:MF_03127}; GN Name=ADSS2 {ECO:0000312|HGNC:HGNC:292}; GN Synonyms=ADSS {ECO:0000255|HAMAP-Rule:MF_03127}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=1592113; DOI=10.1016/0014-5793(92)80465-s; RA Powell S.M., Zalkin H., Dixon J.E.; RT "Cloning and characterization of the cDNA encoding human adenylosuccinate RT synthetase."; RL FEBS Lett. 303:4-10(1992). RN [2] RP SEQUENCE REVISION. RA Stone R.L.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-456 IN COMPLEX WITH GDP. RG Structural genomics consortium (SGC); RT "Human adenylosuccinate synthetase isozyme 2 in complex with GDP."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Plays an important role in the de novo pathway and in the CC salvage pathway of purine nucleotide biosynthesis. Catalyzes the first CC committed step in the biosynthesis of AMP from IMP. CC {ECO:0000250|UniProtKB:P46664}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2- CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03127}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03127}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03127}; CC -!- ACTIVITY REGULATION: Inhibited competitively by AMP and IMP and non- CC competitively by fructose 1,6-bisphosphate. CC {ECO:0000250|UniProtKB:P46664}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03127}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03127}. CC -!- INTERACTION: CC P30520; Q8NB12: SMYD1; NbExp=4; IntAct=EBI-1042898, EBI-8463848; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03127}. CC Mitochondrion {ECO:0000250|UniProtKB:A4Z6H1}. Note=Partially associated CC with particulate fractions. CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_03127}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X66503; CAA47123.1; -; Genomic_DNA. DR EMBL; AL591594; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL645465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471148; EAW77102.1; -; Genomic_DNA. DR EMBL; BC012356; AAH12356.1; -; mRNA. DR CCDS; CCDS1624.1; -. DR PIR; S21166; S21166. DR RefSeq; NP_001117.2; NM_001126.3. DR PDB; 2V40; X-ray; 1.90 A; A=21-456. DR PDBsum; 2V40; -. DR AlphaFoldDB; P30520; -. DR SMR; P30520; -. DR BioGRID; 106668; 111. DR IntAct; P30520; 18. DR MINT; P30520; -. DR STRING; 9606.ENSP00000355493; -. DR BindingDB; P30520; -. DR ChEMBL; CHEMBL4875; -. DR DrugBank; DB00787; Acyclovir. DR DrugBank; DB05540; Alanosine. DR DrugBank; DB00128; Aspartic acid. DR GlyCosmos; P30520; 2 sites, 1 glycan. DR GlyGen; P30520; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P30520; -. DR MetOSite; P30520; -. DR PhosphoSitePlus; P30520; -. DR SwissPalm; P30520; -. DR BioMuta; ADSS; -. DR DMDM; 21264498; -. DR CPTAC; CPTAC-163; -. DR CPTAC; CPTAC-164; -. DR EPD; P30520; -. DR jPOST; P30520; -. DR MassIVE; P30520; -. DR MaxQB; P30520; -. DR PaxDb; 9606-ENSP00000355493; -. DR PeptideAtlas; P30520; -. DR ProteomicsDB; 54711; -. DR Pumba; P30520; -. DR Antibodypedia; 20829; 174 antibodies from 23 providers. DR DNASU; 159; -. DR Ensembl; ENST00000366535.4; ENSP00000355493.3; ENSG00000035687.10. DR GeneID; 159; -. DR KEGG; hsa:159; -. DR MANE-Select; ENST00000366535.4; ENSP00000355493.3; NM_001126.5; NP_001117.2. DR UCSC; uc001iaj.4; human. DR AGR; HGNC:292; -. DR CTD; 159; -. DR DisGeNET; 159; -. DR GeneCards; ADSS2; -. DR HGNC; HGNC:292; ADSS2. DR HPA; ENSG00000035687; Low tissue specificity. DR MIM; 103060; gene. DR neXtProt; NX_P30520; -. DR OpenTargets; ENSG00000035687; -. DR PharmGKB; PA24601; -. DR VEuPathDB; HostDB:ENSG00000035687; -. DR eggNOG; KOG1355; Eukaryota. DR GeneTree; ENSGT00390000015553; -. DR HOGENOM; CLU_029848_3_0_1; -. DR InParanoid; P30520; -. DR OMA; FHHAKPI; -. DR OrthoDB; 122722at2759; -. DR PhylomeDB; P30520; -. DR TreeFam; TF300486; -. DR PathwayCommons; P30520; -. DR Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis. DR SignaLink; P30520; -. DR SIGNOR; P30520; -. DR UniPathway; UPA00075; UER00335. DR BioGRID-ORCS; 159; 347 hits in 1148 CRISPR screens. DR ChiTaRS; ADSS; human. DR EvolutionaryTrace; P30520; -. DR GenomeRNAi; 159; -. DR Pharos; P30520; Tchem. DR PRO; PR:P30520; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P30520; Protein. DR Bgee; ENSG00000035687; Expressed in monocyte and 201 other cell types or tissues. DR ExpressionAtlas; P30520; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0042301; F:phosphate ion binding; NAS:UniProtKB. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IDA:MGI. DR GO; GO:0006167; P:AMP biosynthetic process; IDA:UniProtKB. DR GO; GO:0006531; P:aspartate metabolic process; IEA:Ensembl. DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl. DR GO; GO:0002376; P:immune system process; NAS:UniProtKB. DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central. DR GO; GO:0060359; P:response to ammonium ion; IEA:Ensembl. DR GO; GO:0014074; P:response to purine-containing compound; IEA:Ensembl. DR CDD; cd03108; AdSS; 1. DR Gene3D; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 1. DR Gene3D; 1.10.300.10; Adenylosuccinate Synthetase, subunit A, domain 2; 1. DR Gene3D; 3.90.170.10; Adenylosuccinate Synthetase, subunit A, domain 3; 1. DR HAMAP; MF_00011; Adenylosucc_synth; 1. DR HAMAP; MF_03127; Adenylosucc_synth_vert_acid; 1. DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd. DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS. DR InterPro; IPR042109; Adenylosuccinate_synth_dom1. DR InterPro; IPR042110; Adenylosuccinate_synth_dom2. DR InterPro; IPR042111; Adenylosuccinate_synth_dom3. DR InterPro; IPR001114; Adenylosuccinate_synthetase. DR InterPro; IPR027529; AdSS_2_vert. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00184; purA; 1. DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1. DR PANTHER; PTHR11846:SF13; ADENYLOSUCCINATE SYNTHETASE ISOZYME 2; 1. DR Pfam; PF00709; Adenylsucc_synt; 1. DR SMART; SM00788; Adenylsucc_synt; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1. DR Genevisible; P30520; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; KW Mitochondrion; Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1..456 FT /note="Adenylosuccinate synthetase isozyme 2" FT /id="PRO_0000095130" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 40 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT ACT_SITE 68 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 39..45 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 40..43 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 40 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 65..68 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 67..69 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 67 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 162 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 176 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 255 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 270 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 330..336 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 334 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 336 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127" FT BINDING 362..364 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 444..447 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT VARIANT 179 FT /note="L -> F (in dbSNP:rs12134870)" FT /id="VAR_051881" FT CONFLICT 24..25 FT /note="RP -> A (in Ref. 1; CAA47123)" FT /evidence="ECO:0000305" FT STRAND 30..39 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 43..51 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 55..59 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 68..72 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 75..82 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 103..116 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 126..130 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 138..149 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 166..174 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 181..184 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 188..205 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 213..227 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 234..243 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:2V40" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 277..283 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 290..307 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 316..324 FT /evidence="ECO:0007829|PDB:2V40" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 343..353 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 356..361 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 363..368 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 370..380 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 383..387 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 392..395 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 399..406 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 418..420 FT /evidence="ECO:0007829|PDB:2V40" FT HELIX 423..436 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 440..444 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 446..448 FT /evidence="ECO:0007829|PDB:2V40" FT STRAND 451..454 FT /evidence="ECO:0007829|PDB:2V40" SQ SEQUENCE 456 AA; 50097 MW; 23B7AAC58A238783 CRC64; MAFAETYPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL AQDADIVCRC QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV IHLPGLFEEA EKNVQKGKGL EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ RQEQAGKNLG TTKKGIGPVY SSKAARSGLR MCDLVSDFDG FSERFKVLAN QYKSIYPTLE IDIEGELQKL KGYMEKIKPM VRDGVYFLYE ALHGPPKKIL VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH MINGFTALAL TKLDILDMFT EIKVGVAYKL DGEIIPHIPA NQEVLNKVEV QYKTLPGWNT DISNARAFKE LPVNAQNYVR FIEDELQIPV KWIGVGKSRE SMIQLF //